Identification and characterization of two zebrafish Twik related potassium channels, Kcnk2a and Kcnk2b. Issue 1 (December 2018)

• Record Type: Journal Article
• Authors: Nasr, Nathalie; Faucherre, Adèle; Borsotto, Marc; Heurteaux, Catherine; Mazella, Jean; Jopling, Chris; Moha ou Maati, Hamid
• Is Part Of: Scientific reports. Volume 8:Issue 1(2018)
• Page Start: 1
• Page End: 10
• Publication Date: 2018-12
• Subjects: Natural history -- Research -- Periodicals; Biology -- Research -- Periodicals; Physical sciences -- Research -- Periodicals; Earth sciences -- Research -- Periodicals; Environmental sciences -- Research -- Periodicals; 502.85
• DOI: 10.1038/s41598-018-33664-9
• Languages: English
• ISSNs: 2045-2322

Abstract

Abstract KCNK2 is a 2 pore domain potassium channel involved in maintaining cellular membrane resting potentials. Although KCNK2 is regarded as a mechanosensitive ion channel, it can also be gated chemically. Previous research indicates thatKCNK2 expression is particularly enriched in neuronal and cardiac tissues. In this respect, KCNK2 plays an important role in neuroprotection and has also been linked to cardiac arrhythmias. KCNK2 has subsequently become an attractive pharmacologic target for developing preventative/curative strategies for neuro/cardio pathophysiological conditions. Zebrafish represent an importantin vivo model for rapidly analysing pharmacological compounds. We therefore sought to identify and characterise zebrafishkcnk2 to allow this model system to be incorporated into therapeutic research. Our data indicates that zebrafish possess twokcnk2 orthologs, kcnk2a andkcnk2b . Electrophysiological analysis of both zebrafish Kcnk2 orthologs shows that, like their human counterparts, they are activated by different physiological stimuli such as mechanical stretch, polyunsaturated fatty acids and intracellular acidification. Furthermore, both zebrafish Kcnk2 channels are inhibited by the human KCNK2 inhibitory peptide spadin. Taken together, our results demonstrate that both Kcnk2a and Kcnk2b share similar biophysiological and pharmacological properties to human KCNK2 and indicate that the zebrafish will be a useful model for developing KCNK2 targeting strategies.